Search results for "5-bisphosphate"
showing 10 items of 20 documents
A role for Rho in receptor- and G protein-stimulated phospholipase C Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxi…
1996
Receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins) activate phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-hydrolyzing phospholipase C (PLC) enzymes by activated alpha of free beta gamma subunits of the relevant G proteins. To study whether low molecular weight G proteins of the Rho family are involved in receptor signaling to PLC, we examined the effect of Clostridium difficile toxin B, which glucosylates and thereby inactivates Rho proteins, on the regulation of PLC activity in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor (mAChR) subtype. Toxin B treatment of HEK cells did not affect basal PLC activi…
Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate.
1996
Receptor signalling to phospholipase D (PLD) in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor apparently involves Rho proteins. Since phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] has been recognized as an essential cofactor for PLD activity and since activated Rho proteins have been reported to stimulate the synthesis of PtdIns(4,5)P2, we studied whether in HEK cells PLD activity is regulated by PtdIns(4,5)P2 and, in particular, whether PtdIns(4,5)P2 can restore PLD activity inhibited by Clostridium difficile toxin B, which inactivates Rho proteins. Addition of MgATP to permeabilized HEK cells increased basal PLD activity and potentia…
Modulation of neuronal phospholipase D activity under depolarizing conditions
1999
Neuronal phospholipase D (PLD) activity was hypothesized to be involved in vesicle trafficking and endocytosis and, possibly, transmitter release. We here report that prolonged depolarization of rat hippocampal slices by potassium chloride (KCl) or 4-aminopyridine inhibited PLD activity. Similarly, PLD activity in rat cortical synaptosomes was significantly inhibited by depolarizing agents including veratridine and ouabain. Inhibition of calcium/calmodulin kinase II (CaMKII) which positively modulates synaptosomal PLD activity [Sarri et al. (1998) FEBS Lett. 440, 287-290] by KN-62 caused a further reduction of PLD activity in depolarized synaptosomes. Depolarization-induced inhibition of PL…
Control of cellular phosphatidylinositol 4,5-bisphosphate levels by adhesion signals and Rho GTPases in NIH 3T3 fibroblasts
2000
The involvement of small GTPases of the Rho family in the control of phosphoinositide metabolism by adhesion signals was examined in NIH 3T3 fibroblasts. Abrogation of adhesion signals by detachment of cells from their substratum resulted in a time-dependent decrease in the cellular level of PtdIns(4,5)P2 by approximately 50%. This effect could be mimicked by treatment of adherent cells with Clostridium difficile toxin B and toxin B-1470, which inhibit specific subsets of Rho and Ras GTPases. Detachment of cells that had been pretreated with the clostridial toxins did not cause a further reduction in PtdIns(4,5)P2 levels, suggesting that the target GTPases are integrated into the control of…
Changes in enzymes involved in photosynthesis and other metabolic processes in the fruit of Opuntia ficus-indica during growth and ripening
2011
The aim of this study was to investigate changes in the abundance of a number of enzymes in the peel, core and seeds of fruits of Opuntia ficus-indica (L.) Miller during development. The enzymes studied were phosphoenolpyruvate carboxylase (PEPC; EC: 4.1.1.31), ribulose-1,5-bisphosphate carboxylase/oxygenase (RUBISCO; EC: 4.1.1.39), aldolase (EC: 4.1.2.13), pyruvate, orthophosphate dikinase (PPDK; EC: 2.7.9.1), phosphoenolpyruvate carboxykinase (PEPCK; EC: 4.1.1.49) and aspartate aminotransferase (AspAT; EC: 2.6.1.1). To detect these enzymes, antibodies specific for each enzyme were used to probe Western blots of sodium dodecyl sulphate polyacrylamide gels. Fruit weight increased throughout…
Ribulose-1,5-bisphosphate Carboxylase-Oxygenase: New Aspects Respective the pH-Dependance of the Carboxylation Reaction
1983
The investigation was directed towards the effects of reaction conditions, substrates and pH on the carboxylation reaction of ribulose-1 ,5-bisphosphate carboxylase-oxygenase in the crude enzyme extracts from several plants. Optimal substrate concentrations (HCO3 - and RubP) were determined. The highest carboxylase activity was attained with Tris/HCl buffer. The pH activity profile was quite sharp with an optimum at pH 7.8. Purified and crystallized carboxylase yielded a broad optimum curve under the same reaction conditions
Control of the ribulose 1,5-bisphosphate carboxylase/oxygenase activity by the chloroplastic glutathione pool.
2014
The CO2-fixing activity of ribulose 1,5-bisphosphate carboxylase/oxygenase depends on the redox state of its cysteines. Disulfides like cystamine or 5,5'-dithio-bis(2-nitrobenzoic acid), but not oxidized glutathione, switch the enzyme to the inactive oxidized form. Conversely, thiols like cysteamine, cysteine, dithiotreitol or 2-mercaptoethanol, but not reduced glutathione, recover enzymatic activity after a previous oxidation. Direct regulation of the carboxylase activity by the chloroplastic glutathione pool is hindered by kinetic barriers impeding access to the critical residues. However, reduced glutathione can drive the recovery of activity by means of minute amounts of smaller interme…
Activity and activation state of ribulose-1,5-bisphosphate carboxylase of spruce trees with varying degrees of damage relative to the occurrence of n…
1989
The aim was to determine whether a reduced carboxylation efficiency in needles of damaged spruce trees (Picea abies), is derived from a direct impairment of the ribulose-1,5-bisphosphate carboxylase (RuBP carboxylase) or there is an indirect inhibition of the RuBP carboxylase. In 1985, 1986 and 1987 measurements of RuBP carboxylase activity were carried out at three locations. Trees of different ages and degrees of damage were examined. RuBP carboxylase was assayed using both a rapid extraction method to determine the initial activity and an in vitro test after total activation to determine the total activity. The activation state was calculated as the ratio of initial activity to total act…
Effect of Glufosinate (Phosphinothricin) and Inhibitors of Photorespiration on Photosynthesis and Ribulose-1,5-Bisphosphate Carboxylase Activity
1992
Summary Glufosinate (phosphinothricin) irreversibly inhibits glutamine synthetase and leads to a great decrease in the amino acids glutamine, glutamate, aspartate, serine, glycine and alanine. Due to the lack of glutamate and serine, the transamination of glyoxylate into glycine in the course of photorespiration cannot take place. The inhibition of this part of the photorespiratory process plays the essential role with respect to the photosynthesis inhibition caused by PPT under atmospheric conditions. After addition of different photorespiration or Calvin cycle intermediates to phosphinothricin no decrease in photosynthesis inhibition can be measured. This suggests that photosynthesis inhi…
Reversible inhibition of CO2fixation by ribulose 1,5-bisphosphate carboxylase/oxygenase through the synergic effect of arsenite and a monothiol
2013
The activity of the photosynthetic carbon-fixing enzyme, ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), is partially inhibited by arsenite in the millimolar concentration range. However, micromolar arsenite can fully inhibit Rubisco in the presence of a potentiating monothiol such as cysteine, cysteamine, 2-mercaptoethanol or N-acetylcysteine, but not glutathione. Arsenite reacts specifically with the vicinal Cys172-Cys192 from the large subunit of Rubisco and with the monothiol to establish a ternary complex, which is suggested to be a trithioarsenical. The stability of the complex is strongly dependent on the nature of the monothiol. Enzyme activity is fully recovered through …